BMRBj - BMREntryMaster

	Total	¹H	¹³C	¹⁵N
All	62.5 % (678 of 1085)	78.2 % (437 of 559)	38.2 % (162 of 424)	77.5 % (79 of 102)
Backbone	69.6 % (398 of 572)	82.1 % (161 of 196)	56.0 % (159 of 284)	84.8 % (78 of 92)
Sidechain	58.7 % (354 of 603)	76.0 % (276 of 363)	33.5 % (77 of 230)	10.0 % (1 of 10)
Aromatic	34.3 % (37 of 108)	66.7 % (36 of 54)	0.0 % (0 of 53)	100.0 % (1 of 1)
Methyl	61.1 % (55 of 90)	97.8 % (44 of 45)	24.4 % (11 of 45)

1. Antivirulence protein AVR-Pia

APQDNTSMGS SHHHHHHSSG RENLYFQGHM AAPARSCVYY DGHLPATRVL LMYVRIGNTA TITARGHEFE VEAKDQNCKV ILTNGKQAPD WLAAEPY

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 305 K, pH 5.4, Details 1 mM [U-15N] AVR-Pia-H3, 90% H2O/10% D2O

#	Name	Isotope labeling	Concentration
1	AVR-Pia-H3	[U-15N]	1 mM
2	H2O	natural abundance	90 %
3	D2O	natural abundance	10 %

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	internal	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.1013291

Referencing offset: 0.1 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	internal	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.1013291

Referencing offset: 0.1 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	internal	indirect	0.2514495
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	internal	indirect	0.1013291

Referencing offset: 0.0 ppm, Outliers: 3 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 5JHJ, Strand ID: A Detail

Release date

2016-04-20

Citation

Recognition of the Magnaporthe oryzae Effector AVR-Pia by the Decoy Domain of the Rice NLR Immune Receptor RGA5
Ortiz, D., de Guillen, K., Cesari, S., Chalvon, V., Gracy, J., Padilla, A., Kroj, T.
Plant Cell (2017), 29, 156-168, PubMed 28087830 , DOI 10.1105/tpc.16.00435 , Abstract

Experiments performed 6 experiments Detail

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_30068_5jhj.nef
Input source #2: Coordindates	5jhj.cif
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	True (see coordinates for details)
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
A:25:CYS:SG	A:66:CYS:SG	oxidized, CA 53.34, CB 40.08 ppm	oxidized, CA 55.14, CB 36.57 ppm	2.032

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

--------------------10--------20--------30--------40--------50--------60--------70--------80-----
APQDNTSMGSSHHHHHHSSGRENLYFQGHMAAPARSCVYYDGHLPATRVLLMYVRIGNTATITARGHEFEVEAKDQNCKVILTNGKQAPDWLAAEPY
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
APQDNTSMGSSHHHHHHSSGRENLYFQGHMAAPARSCVYYDGHLPATRVLLMYVRIGNTATITARGHEFEVEAKDQNCKVILTNGKQAPDWLAAEPY
--------10--------20--------30--------40--------50--------60--------70--------80--------90-------

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	97	0	0	100.0

Content subtype: combined_30068_5jhj.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Covalent bonds	assembly	OK	1		No information
1	Assigned chemical shifts	assigned_chemical_shifts_1	Warning	659		81.4 (chain: A, length: 97)
1	Distance restraints	CNS/XPLOR_distance_constraints_4	Warning	1567 (1)	noe	81.4 (chain: A, length: 97)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	Warning	20 (1)	hbond	28.9 (chain: A, length: 97)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_2	OK	106 (106)	.	67.0 (chain: A, length: 97)

Assigned chemical shifts

Saveframe: assigned_chemical_shifts_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 97, Sequence coverage: 81.4%
- Total number of assignments
  - ¹H chemical shifts: 432
  - ¹³C chemical shifts: 152
  - ¹⁵N chemical shifts: 75
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- Peptide bond of PRO
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: A

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	559	432	77.3
¹³C chemical shifts	424	152	35.8
¹⁵N chemical shifts	107	75	70.1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	196	159	81.1
¹³C chemical shifts	194	79	40.7
¹⁵N chemical shifts	92	75	81.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	363	273	75.2
¹³C chemical shifts	230	73	31.7
¹⁵N chemical shifts	15	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	48	45	93.8
¹³C chemical shifts	48	10	20.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	54	36	66.7
¹³C chemical shifts	53	0	0.0
¹⁵N chemical shifts	1	0	0.0

Covalent bonds

Saveframe: assembly
- Status: OK

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_4
- Status: Warning
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 97, Sequence coverage: 81.4%
- Total number of restraints: 1567
- Weight of restraints: 1.0 (1567)
- Potential type of restraints: square-well-parabolic (1567)
- Range of distance target values: 2.0, 5.65 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_3
  - Status: Warning
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 97, Sequence coverage: 28.9%
  - Total number of restraints: 20
  - Weight of restraints: 1.0 (20)
  - Potential type of restraints: square-well-parabolic (20)
  - Range of distance target values: 2.1, 2.1 (Å)
  - Distance restraints per residue
    - Chain_ID: A
  - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_2
- Status: OK
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 97, Sequence coverage: 67.0%
- Total number of restraints: 106
- Total number of restraints per polymer type: 106
- Weight of restraints: 1.0 (106)
- Potential type of restraints: square-well-parabolic (106)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue
  - Chain_ID: A

Keywords Avirulence effector Magnaporthe Oryzae, Structure from MOLMOL, antiviral

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BMRB: 30068

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Experiments performed 6 experiments Detail

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NMR combined restraints 5 contents Detail